| 词条 | Proton-pumping pyrophosphatase |
| 释义 |
| Symbol = H_PPase | Name = Inorganic H+ pyrophosphatase | image = | width = | caption = | Pfam = PF03030 | Pfam_clan = | InterPro = IPR004131 | SMART = | PROSITE = | MEROPS = | SCOP = | TCDB = 3.A.10 | OPM family = 390 | OPM protein = 4a01 | CAZy = | CDD = }} Two types of inorganic diphosphatase, very different in terms of both amino acid sequence and structure, have been characterised to date: soluble and transmembrane proton-pumping pyrophosphatases (sPPases and H(+)-PPases, respectively). sPPases are ubiquitous proteins that hydrolyse pyrophosphate to release heat, whereas H+-PPases, so far unidentified in animal and fungal cells, couple the energy of PPi hydrolysis to proton movement across biological membranes.[1][2] The latter type is represented by this group of proteins. H+-PPases are also called vacuolar-type inorganic pyrophosphatases (V-PPase) or pyrophosphate-energised vacuolar membrane proton pumps.[3] In plants, vacuoles contain two enzymes for acidifying the interior of the vacuole, the V-ATPase and the V-PPase (V is for vacuolar).[2] Two distinct biochemical subclasses of H+-PPases have been characterised to date: K+-stimulated and K+-insensitive.[1][3] References1. ^1 {{cite journal |vauthors=Perez-Castineira JR, Lopez-Marques RL, Villalba JM, Losada M, Serrano A | title = Functional complementation of yeast cytosolic pyrophosphatase by bacterial and plant H+-translocating pyrophosphatases | journal = Proc. Natl. Acad. Sci. U.S.A. | volume = 99 | issue = 25 | pages = 15914–9 |date=December 2002 | pmid = 12451180 | pmc = 138539 | doi = 10.1073/pnas.242625399 | url = | hdl = 11441/26079 }} {{InterPro content|IPR004131}}2. ^1 {{cite journal |vauthors=Baltscheffsky M, Schultz A, Baltscheffsky H | title = H+ -PPases: a tightly membrane-bound family | journal = FEBS Lett. | volume = 457 | issue = 3 | pages = 527–33 |date=September 1999 | pmid = 10523139 | doi = 10.1016/S0014-5793(99)90617-8| url = }} 3. ^1 {{cite journal |vauthors=Perez-Castineira JR, Lopez-Marques RL, Losada M, Serrano A | title = A thermostable K(+)-stimulated vacuolar-type pyrophosphatase from the hyperthermophilic bacterium Thermotoga maritima | journal = FEBS Lett. | volume = 496 | issue = 1 | pages = 6–11 |date=May 2001 | pmid = 11343697 | doi = 10.1016/S0014-5793(01)02390-0| url = }} 2 : Protein families|Transmembrane proteins |
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